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Self-assemblingpeptides can be used to create tunable higher-orderstructures for the multivalent presentation of a variety of ligands.We describe a novel, fiber-forming coiled-coil-based peptide thatassembles to display, simultaneously, carbohydrate and peptide ligandsrecognized by biomacromolecules. Preassembly decoration of the scaffoldwith a diphtheria toxin peptide epitope or a mannose motif did notinterfere with self-assembly of the nanostructure. The resulting multivalentdisplay led to tighter binding by antidiphtheria toxin antibodiesand mannose-specific carbohydrate binding proteins, respectively.The potential of this self-assembling peptide to display ligands inbioanalytical assays is illustrated by its decoration with a disaccharideglycotope from the Leishmaniaparasite.Carbohydrate-specific antibodies produced in response to a Leishmaniainfection are detected more sensitivelyin human and canine sera due to the multivalent presentation on theself-assembled scaffold. Thus, nanofibers based on coiled-coil peptidesare a powerful tool for the development of bioassays and diagnostics. [ABSTRACT FROM AUTHOR]